General Information
-
DRAMP ID
- DRAMP03664
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Peptide Name
- L-amino-acid oxidase (LAAO, LAO, TM-LAO; reptilia, animals)
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Source
- Trimeresurus mucrosquamatus (Taiwan habu) (Protobothrops mucrosquamatus)
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Family
- Not found
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Gene
- Not found
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Sequence
- ADNKNPLEECFRETNYEEFLEIAR
-
Sequence Length
- 24
-
UniProt Entry
- P0C2D6
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Protein Existence
- Protein level
Activity Information
-
Biological Activity
- Antimicrobial, Antibacterial, Anti-Gram-
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Target Organism
-
- Gram-negative bacterium: E. coli;
- S. aureus, B. dysenteriae.
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Hemolytic Activity
-
- No hemolysis information or data found in the reference(s) presented in this entry
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Cytotoxicity
-
- Not included yet
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Binding Target
- Not found
Structure Information
-
Linear/Cyclic
- Not included yet
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N-terminal Modification
- Not included yet
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C-terminal Modification
- Not included yet
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Nonterminal Modifications and Unusual Amino Acids
- Not included yet
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Stereochemistry
- Not included yet
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Structure
- Not found
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Structure Description
- Not found
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Helical Wheel Diagram
-
PDB ID
- None
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Predicted Structure
- There is no predicted structure for DRAMP03664.
Physicochemical Information
-
Formula
- C127H192N34O44S
Absent Amino Acids
- GHMQSVW
Common Amino Acids
- E
Mass
- 2931.18
PI
- 4.31
Basic Residues
- 3
Acidic Residues
- 7
Hydrophobic Residues
- 7
Net Charge
- -4
-
Boman Index
- -81.98
Hydrophobicity
- -1.154
Aliphatic Index
- 57.08
Half Life
-
- Mammalian:4.4 hour
- Yeast:>20 hour
- E.coli:>10 hour
Extinction Coefficient Cystines
- 1490
Absorbance 280nm
- 64.78
Polar Residues
- 6
DRAMP03664
Comments Information
Function
- Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Exhibits diverse biological activities, such as hemorrhage, hemolysis, edema, apoptosis, and antiparasitic activities By similarity. This protein has antibacterial activity abd cytotoxic activity, as well as an ability to induce platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions.
Tissue specificity
- Expressed by the venom gland. PTM
Literature Information
- ·Literature 1
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Title
- Purification, characterization and biological activity of an L-amino acid oxidase from Trimeresurus mucrosquamatus venom.
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Pubmed ID
- 12621545
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Reference
- Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2003 Mar;35(3):219-224.
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Author
- Wei JF, Wei Q, Lu QM, Tai H, Jin Y, Wang WY, Xiong YL.